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p38β Kinase Enzyme System

 
包装: 10μg
运保温度: -70℃
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描述:

Recombinant full-length human p38β was expressed by baculovirus in Sf9 insect cells using an N-terminal GST tag. p38β is a member of the p38 MAP kinase family and is activated by both proinflammatory cytokines and environmental stress (1). The p38β is activated through its phosphorylation by MAP kinase kinases (MKKs), preferably by MKK6. Transcription factor ATF2/CREB2 has been shown to be a substrate of this kinase (2). Alternatively spliced transcript variants encoding the same protein have been observed.

 

ADP-Glo™ Kinase Assay is a luminescent kinase assay that measures ADP formed from a kinase reaction; ADP is converted into ATP, which is a substrate in a reaction catalyzed by Ultra-Glo™ Luciferase that produces light. The luminescent signal positively correlates with ADP amount and kinase activity. The assay is well suited for measuring the effects chemical compounds have on the activity of a broad range of purified kinases, making it ideal for both primary screening as well as kinase selectivity profiling. The ADP-Glo™ Kinase Assay can be used to monitor the activity of virtually any ADP-generating enzyme (e.g., kinase or ATPase) using up to 1mM ATP.

 

Kinase Enzyme System contains:

Kinase: p38β, 10μg (Human, recombinant full-length). MW: ~71kDa.
Substrate: p38 substrate (IPTTPITTTYFFFKKK).
Other: Reaction Buffer, DTT.

p38β NCBI Database Entry.

Human Kinase Enzyme Systems and Applications.

Features - Benefits

Profile More Compounds In-House: ADP-Glo™ Kinase Assay + Kinase Enzyme System is optimized so that you are up and running in no time.
Complete Systems: The Kinase Enzyme Systems include a recombinant kinase enzyme, a substrate appropriate for the enzyme, a reaction buffer, DTT and supplemental reagents as needed.
Obtain Reliable Results: The broad dynamic range, the ease of use and better sensitivity obtained with ADP-Glo™ Kinase Assay result in less ambiguous data.

 

Notes

Kinase Enzyme System manufactured by SignalChem.
Bulk quantities available upon request.

 

References

1.Jiang, Y. et al. (1996) Characterization of the structure and function of a new mitogen-activated protein kinase (p38-beta). J. Biol. Chem. 271, 17920–6.
2.Stein, B. et al. (1997) p38-2, a novel mitogen-activated protein kinase with distinct properties. J. Biol. Chem. 272, 19509–17.


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